ID Q1KLC3_CITFR Unreviewed; 552 AA.
AC Q1KLC3;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:ABF06666.1};
DE EC=2.7.1.29 {ECO:0000313|EMBL:ABF06666.1};
GN Name=dhaK {ECO:0000313|EMBL:ABF06666.1};
OS Citrobacter freundii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546 {ECO:0000313|EMBL:ABF06666.1};
RN [1] {ECO:0000313|EMBL:ABF06666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CECT 4626 {ECO:0000313|EMBL:ABF06666.1};
RX PubMed=15263954; DOI=10.1039/b405220j;
RA Sanchez-Moreno I., Garcia-Garcia J.F., Bastida A., Garcia-Junceda E.;
RT "Multienzyme system for dihydroxyacetone phosphate-dependent aldolase
RT catalyzed C-C bond formation from dihydroxyacetone.";
RL Chem. Commun. (Camb.) 14:1634-1635(2004).
RN [2] {ECO:0000313|EMBL:ABF06666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CECT 4626 {ECO:0000313|EMBL:ABF06666.1};
RA Sanchez-Moreno I., Martin-Hoyos R., Garcia-Junceda E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DQ473522; ABF06666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KLC3; -.
DR BRENDA; 2.7.1.29; 1398.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR NCBIfam; TIGR02361; dak_ATP; 1.
DR PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABF06666.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABF06666.1}.
FT DOMAIN 8..327
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 356..548
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 220
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 552 AA; 58021 MW; 257973CBCBE2DF56 CRC64;
MSQFFFNQRT HLVSDVIDGT IIASPWNNLA RLESDPAIRI VVRRDLNKNN VAVISGGGSG
HEPAHVGFIG KGMLTAAVCG DVFASPSVDA VLTAIQAVTG EAGCLLIVKN YTGDRLNFGL
AAEKARRLGY NVEMLIVGDD ISLPDNKHPR GIAGTILVHK IAGYFAERGY NLATVLREAQ
YAANNTFSLG VALSSCHLPQ EADAAPRHHP GHAELGMGIH GEPGASVIDT QNSAQVVNLM
VDKLMAALPE TGRLAVMINN LGGVSVAEMA IITRELASSP LHPRIDWLIG PASLVTALDM
KSFSLTAIVL EESIEKALLT EVETSNWPTP VPPREISCVP SSQRSARVEF QPSANAMVAG
IVELVTTTLS DLETHLNALD AKVGDGDTGS TFAAGAREIA SLLHRQQLPL DNLATLFALI
GERLTVVMGG SSGVLMSIFF TAAGQKLEQG ASVAESLNTG LAQMKFYGGA DEGDRTMIDA
LQPALTSLLT QPQNLQAAFD AAQAGAERTC LSSKANAGRA SYLSSESLLG NMDPGAHAVA
MVFKALAESE LG
//
